The differential expression patterns of group IIA, III, V and X sPLA2s suggest a potential role for sPLA2s in human breast cancer and indicate that different sPLA2s may have distinct roles at different levels of progression of the disease. Our results show that overexpression of group X sPLA2 in the highly invasive MDA-MB-231 breast cancer cells causes a significant decrease in their proliferation rate and invasive potential. Exogenously added recombinant human group X sPLA2 induces a time- and concentration-dependent decrease of the rate of proliferation of MDA-MB-231 cells.
COBISS.SI-ID: 22962471
sPLA2-X was for the first time produced in bacteria as a non-fused protein, only with the initial Met residue preceding the first amino acid residue, Gly, of the mature enzyme. Despite of our expectation, the Met at position -1 has not been completely removed in vivo. However, we were able to separate the properly processed recombinant sPLA2-X from the Met form by including an additional purification step of a calmodulin-affinity column before the final reversed-phase HPLC purification. Both sPLA2s were active at releasing free fatty acids from the intact membranes of mammalian cell lines.
COBISS.SI-ID: 22961447